Literature summary extracted from

Sramek, S.J.; Frerman, F.E.
Escherichia coli coenzyme A-transferase: kinetics, catalytic pathway and structure (1975), Arch. Biochem. Biophys., 171, 27-35.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.8.3.9	epsilon-Acetyl-CoA	-	Escherichia coli
2.8.3.9	NaBH4	-	Escherichia coli

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.8.3.9	0.035	-	acetoacetyl-CoA	pH 8.1, 25°C	Escherichia coli
2.8.3.9	0.26	-	acetyl-CoA	pH 8.1, 25°C	Escherichia coli

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
2.8.3.9	23000	-	2 * 23000 + 2 * 26000, 2 alpha and 2 beta subunits, SDS-PAGE	Escherichia coli
2.8.3.9	26000	-	2 * 23000 + 2 * 26000, 2 alpha and 2 beta subunits, SDS-PAGE	Escherichia coli
2.8.3.9	97000	-	gel filtration	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.8.3.9	Escherichia coli	-	C22	-
2.8.3.9	Escherichia coli C22	-	C22	-

Subunits

EC Number	Subunits	Comment	Organism
2.8.3.9	tetramer	2 * 23000 + 2 * 26000, 2 alpha and 2 beta subunits, SDS-PAGE	Escherichia coli

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
2.8.3.9	10.6	-	epsilon-Acetyl-CoA	-	Escherichia coli

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Release 2023.1 (January 2023)